ID A0A2P6TUA4_CHLSO Unreviewed; 403 AA.
AC A0A2P6TUA4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Thioredoxin chloroplastic {ECO:0000313|EMBL:PRW57641.1};
GN ORFNames=C2E21_3600 {ECO:0000313|EMBL:PRW57641.1};
OS Chlorella sorokiniana (Freshwater green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW57641.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW57641.1, ECO:0000313|Proteomes:UP000239899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004477}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the DPM3 family.
CC {ECO:0000256|ARBA:ARBA00010430}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PRW57641.1}.
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DR EMBL; LHPG02000006; PRW57641.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6TUA4; -.
DR STRING; 3076.A0A2P6TUA4; -.
DR OrthoDB; 45858at2759; -.
DR Proteomes; UP000239899; Unassembled WGS sequence.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro.
DR CDD; cd09212; PUB; 1.
DR CDD; cd02947; TRX_family; 1.
DR Gene3D; 1.20.58.2190; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR013174; DPM3.
DR InterPro; IPR036339; PUB-like_dom_sf.
DR InterPro; IPR018997; PUB_domain.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR InterPro; IPR017937; Thioredoxin_CS.
DR InterPro; IPR013766; Thioredoxin_domain.
DR PANTHER; PTHR46115:SF5; THIOREDOXIN DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46115; THIOREDOXIN-LIKE PROTEIN 1; 1.
DR Pfam; PF08285; DPM3; 1.
DR Pfam; PF09409; PUB; 1.
DR Pfam; PF00085; Thioredoxin; 1.
DR PRINTS; PR00421; THIOREDOXIN.
DR SMART; SM00580; PUG; 1.
DR SUPFAM; SSF143503; PUG domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS00194; THIOREDOXIN_1; 1.
DR PROSITE; PS51352; THIOREDOXIN_2; 1.
PE 3: Inferred from homology;
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000239899};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..403
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015173603"
FT TRANSMEM 37..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 76..188
FT /note="Thioredoxin"
FT /evidence="ECO:0000259|PROSITE:PS51352"
FT REGION 327..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 384..403
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 403 AA; 41673 MW; 1AD3C5902B3C6393 CRC64;
MLRIVRLGLL LAVLLAAWVA LLQRTAGEEA IHTAVLLAPL AAVVLFGAVL VCQLLYGVAT
FRTVPEEAEL LQKDIARAKA ELGSSELQTI LGAAARRSQL VLVDFSASWC GPCRMMLPVL
QQLAQELCGR LAVVKVDCEQ TSANQALASS SGIRAFPTFH LYRAQQKVGE LRGADPAGLR
RAIDQQLALL GPSSGGASTS GGASGMSAAG MAMCNALAQA LARVKAGCSY DEFVAAAKTL
LTFVSNVIDQ PGEEKFRRVK ASNAAYQSKL GCRPGGKEAM AAIGFKEMME AGEAVLVMNE
VPSELPRVRQ LLQSALQQAE AAAAAMGGRG SSGTSAAGAR PAAGAAGGAG TAAGRQRIVR
VTPRKLAKVL EKCLAEVGVG QVAQQAQQAQ QTQQEGSQGG GQP
//
